1mp6: Difference between revisions
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[[ | ==Structure of the transmembrane region of the M2 protein H+ channel by solid state NMR spectroscopy== | ||
<StructureSection load='1mp6' size='340' side='right' caption='[[1mp6]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1mp6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MP6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MP6 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mp6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1mp6 RCSB], [http://www.ebi.ac.uk/pdbsum/1mp6 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The transmembrane domain of the M2 protein from influenza A virus forms a nearly uniform and ideal helix in a liquid crystalline bilayer environment. The exposure of the hydrophilic backbone structure is minimized through uniform hydrogen bond geometry imposed by the low dielectric lipid environment. A high-resolution structure of the monomer backbone and a detailed description of its orientation with respect to the bilayer were achieved using orientational restraints from solid-state NMR. With this unique information, the tetrameric structure of this H(+) channel is constrained substantially. Features of numerous published models are discussed in light of the experimental structure of the monomer and derived features of the tetrameric bundle. | |||
Structure of the transmembrane region of the M2 protein H(+) channel.,Wang J, Kim S, Kovacs F, Cross TA Protein Sci. 2001 Nov;10(11):2241-50. PMID:11604531<ref>PMID:11604531</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Ion channels|Ion channels]] | *[[Ion channels|Ion channels]] | ||
*[[M2 protein|M2 protein]] | *[[M2 protein|M2 protein]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Cross, T A.]] | [[Category: Cross, T A.]] | ||
[[Category: Kim, S.]] | [[Category: Kim, S.]] | ||
Revision as of 16:39, 28 September 2014
Structure of the transmembrane region of the M2 protein H+ channel by solid state NMR spectroscopyStructure of the transmembrane region of the M2 protein H+ channel by solid state NMR spectroscopy
Structural highlights
Publication Abstract from PubMedThe transmembrane domain of the M2 protein from influenza A virus forms a nearly uniform and ideal helix in a liquid crystalline bilayer environment. The exposure of the hydrophilic backbone structure is minimized through uniform hydrogen bond geometry imposed by the low dielectric lipid environment. A high-resolution structure of the monomer backbone and a detailed description of its orientation with respect to the bilayer were achieved using orientational restraints from solid-state NMR. With this unique information, the tetrameric structure of this H(+) channel is constrained substantially. Features of numerous published models are discussed in light of the experimental structure of the monomer and derived features of the tetrameric bundle. Structure of the transmembrane region of the M2 protein H(+) channel.,Wang J, Kim S, Kovacs F, Cross TA Protein Sci. 2001 Nov;10(11):2241-50. PMID:11604531[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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